ID   SYGB_NEIG2              Reviewed;         687 AA.
AC   B4RJG3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE            EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00255};
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE            Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00255};
GN   Name=glyS {ECO:0000255|HAMAP-Rule:MF_00255}; OrderedLocusNames=NGK_2629;
OS   Neisseria gonorrhoeae (strain NCCP11945).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=521006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCCP11945;
RX   PubMed=18586945; DOI=10.1128/jb.00566-08;
RA   Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT   "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL   J. Bacteriol. 190:6035-6036(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC         tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC         COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC         EC=6.1.1.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00255};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00255}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00255}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00255}.
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DR   EMBL; CP001050; ACF31228.1; -; Genomic_DNA.
DR   RefSeq; WP_012504125.1; NC_011035.1.
DR   AlphaFoldDB; B4RJG3; -.
DR   SMR; B4RJG3; -.
DR   EnsemblBacteria; ACF31228; ACF31228; NGK_2629.
DR   KEGG; ngk:NGK_2629; -.
DR   HOGENOM; CLU_007220_2_2_4; -.
DR   OMA; LPIPKRM; -.
DR   OrthoDB; 213210at2; -.
DR   Proteomes; UP000002564; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   TIGRFAMs; TIGR00211; glyS; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..687
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000101307"
SQ   SEQUENCE   687 AA;  74468 MW;  91008E2EC8F44522 CRC64;
     MTTQTLLIEL LTEELPPKAL NNLGNHFAAS VAEGLEKAQL VDGAAEFTAY ASPRRLAVQV
     KNVKAVQADQ KIVKKGPAVA NAVKDGTPTK ALEGFARGAG AKIEDLTIIH DGRQDVYAYE
     YVQTGRPLGG LLEDIINQAV KKLPIPKVMR WGSSTFTFVR PVHGLIVLHG GDVVNVSVLG
     LQSGNQTLGH RFLSDGEIII ENADSYAAQM RGQGKVVASF AGRKAAIQTA LEGQARRLNA
     TVAADEALLD EVTALVEWPV VLEAGFEEHF LAMPQECLIL TMQQNQKYFP LLDQNGKLMN
     RFLLVSNLQT EDPSHIIRGN ERVLRARLSD AEFFYKQDQK ATLESRLPKL ANVVYHNKIG
     SQAERIERLQ SIAAHIAKAL GADAAAAGRA ARLAKADLVT EMVGEFPELQ GTMGKYYARL
     DGETEEIAEA IEQHYQPRFA GDKLPESKIA AAVALADKLE TLVGIWGIGL IPTGDKDPYA
     LRRAALGILR MLMQYGLDVN ELIQTAFDSF PQGLLNEKTP SETADFMQAR LAVLLQNDYP
     QDIVAAVLAK QPRRLDDLTA KLQAVAVFKQ LPEAAALAAA NKRVQNLLKK ADAALGAVNE
     SLLQQDEEKA LYAAAQGLQP KIAAAVAEGN FRTALSELAS VKPQVDAFFD GVMVMAEDAA
     VKQNRLNLLN RLAEQMNAVA DIALLGE